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Q6UVK1 (CSPG4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chondroitin sulfate proteoglycan 4
Alternative name(s):
Chondroitin sulfate proteoglycan NG2
Melanoma chondroitin sulfate proteoglycan
Melanoma-associated chondroitin sulfate proteoglycan
Gene names
Name:CSPG4
Synonyms:MCSP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2322 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Proteoglycan playing a role in cell proliferation and migration which stimulates endothelial cells motility during microvascular morphogenesis. May also inhibit neurite outgrowth and growth cone collapse during axon regeneration. Cell surface receptor for collagen alpha 2(VI) which may confer cells ability to migrate on that substrate. Binds through its extracellular N-terminus growth factors, extracellular matrix proteases modulating their activity. May regulate MPP16-dependent degradation and invasion of type I collagen participating in melanoma cells invasion properties. May modulate the plasminogen system by enhancing plasminogen activation and inhibiting angiostatin. Functions also as a signal transducing protein by binding through its cytoplasmic C-terminus scaffolding and signaling proteins. May promote retraction fiber formation and cell polarization through Rho GTPase activation. May stimulate alpha-4, beta-1 integrin-mediated adhesion and spreading by recruiting and activating a signaling cascade through CDC42, ACK1 and BCAR1. May activate FAK and ERK1/ERK2 signaling cascades. Ref.2 Ref.6 Ref.7

Subunit structure

Interacts with the first PDZ domain of MPDZ. Interacts with PRKCA. Binds TNC, laminin-1, COL5A1 and COL6A2. Interacts with PLG and angiostatin. Binds FGF2 and PDGFA. Interacts with GRIP1, GRIP2 and GRIA2. Forms a ternary complex with GRIP1 and GRIA2 By similarity. Interacts with LGALS3 and the integrin composed of ITGB1 and ITGA3. Interacts with ITGA4 through its chondroitin sulfate glycosaminoglycan. Interacts with BCAR1, CDC42 and ACK1. Interacts with MMP16. Ref.5 Ref.6 Ref.7 Ref.9

Subcellular location

Apical cell membrane; Single-pass type I membrane protein; Extracellular side By similarity. Cell projectionlamellipodium membrane; Single-pass type I membrane protein; Extracellular side By similarity. Note: Localized at the apical plasma membrane it relocalizes to the lamellipodia of astrocytoma upon phosphorylation by PRKCA. Localizes to the retraction fibers. Localizes to the plasma membrane of oligodendrocytes By similarity.

Tissue specificity

Detected only in malignant melanoma cells. Ref.1

Post-translational modification

O-glycosylated; contains glycosaminoglycan chondroitin sulfate which are required for proper localization and function in stress fiber formation By similarity. Involved in interaction with MMP16 and ITGA4.

Phosphorylation by PRKCA regulates its subcellular location and function in cell motility By similarity.

Miscellaneous

Valuable marker for several incompletely differentiated precursor cells.

Sequence similarities

Contains 15 CSPG (NG2) repeats.

Contains 2 laminin G-like domains.

Ontologies

Keywords
   Biological processAngiogenesis
Differentiation
Tissue remodeling
   Cellular componentCell membrane
Cell projection
Membrane
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
Transducer
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Proteoglycan
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPK activity

Inferred from electronic annotation. Source: Ensembl

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

carbohydrate metabolic process

Traceable author statement. Source: Reactome

cell proliferation

Inferred from electronic annotation. Source: Ensembl

chondroitin sulfate biosynthetic process

Traceable author statement. Source: Reactome

chondroitin sulfate catabolic process

Traceable author statement. Source: Reactome

chondroitin sulfate metabolic process

Traceable author statement. Source: Reactome

dermatan sulfate biosynthetic process

Traceable author statement. Source: Reactome

glial cell migration

Inferred from electronic annotation. Source: Ensembl

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

intracellular signal transduction

Inferred from direct assay Ref.6. Source: UniProtKB

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.6. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

tissue remodeling

Inferred from electronic annotation. Source: UniProtKB-KW

transmembrane receptor protein tyrosine kinase signaling pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi lumen

Traceable author statement. Source: Reactome

apical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell surface

Traceable author statement Ref.6. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

lamellipodium membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

lysosomal lumen

Traceable author statement. Source: Reactome

   Molecular_functionprotein kinase binding

Inferred from physical interaction Ref.6. Source: UniProtKB

signal transducer activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 23222293Chondroitin sulfate proteoglycan 4
PRO_0000041962

Regions

Topological domain30 – 22242195Extracellular Potential
Transmembrane2225 – 224521Helical; Potential
Topological domain2246 – 232277Cytoplasmic Potential
Domain30 – 192163Laminin G-like 1
Domain202 – 380179Laminin G-like 2
Repeat430 – 52394CSPG 1
Repeat556 – 64388CSPG 2
Repeat665 – 764100CSPG 3
Repeat792 – 87887CSPG 4
Repeat900 – 98990CSPG 5
Repeat1020 – 110889CSPG 6
Repeat1128 – 121689CSPG 7
Repeat1241 – 133797CSPG 8
Repeat1360 – 144990CSPG 9
Repeat1476 – 156186CSPG 10
Repeat1583 – 167997CSPG 11
Repeat1707 – 180397CSPG 12
Repeat1835 – 192288CSPG 13
Repeat1944 – 202986CSPG 14
Repeat2048 – 2147100CSPG 15
Region30 – 639610Globular or compact configuration stabilized by disulfide bonds
Region30 – 639610Neurite growth inhibition By similarity
Region574 – 1040467Interaction with COL6A2 By similarity
Region631 – 1446816Interaction with COL5A1 By similarity
Region1586 – 2221636Neurite growth inhibition By similarity
Region1587 – 2221635Cysteine-containing
Motif2320 – 23223PDZ-binding
Compositional bias639 – 1586948Gly/Ser-rich (glycosaminoglycan attachment domain)

Amino acid modifications

Modified residue22521Phosphothreonine; by PKC/PRKCA By similarity
Glycosylation1301N-linked (GlcNAc...) Potential
Glycosylation3481N-linked (GlcNAc...) Potential
Glycosylation4271N-linked (GlcNAc...) Potential
Glycosylation6851N-linked (GlcNAc...) Potential
Glycosylation7721N-linked (GlcNAc...) Potential
Glycosylation9951O-linked (Xyl...) (chondroitin sulfate) By similarity
Glycosylation11311N-linked (GlcNAc...) Potential
Glycosylation12021N-linked (GlcNAc...) Potential
Glycosylation13641N-linked (GlcNAc...) Potential
Glycosylation14491N-linked (GlcNAc...) Potential
Glycosylation16451N-linked (GlcNAc...) Potential
Glycosylation19091N-linked (GlcNAc...) Potential
Glycosylation20161N-linked (GlcNAc...) Potential
Glycosylation20341N-linked (GlcNAc...) Potential
Glycosylation20401N-linked (GlcNAc...) Potential
Glycosylation20751N-linked (GlcNAc...) Ref.10
Disulfide bond169 ↔ 192 By similarity
Disulfide bond354 ↔ 380 By similarity

Natural variations

Natural variant17031R → H.
Corresponds to variant rs8023621 [ dbSNP | Ensembl ].
VAR_061733

Experimental info

Sequence conflict5 – 62PR → RG in CAA65529. Ref.1
Sequence conflict5 – 62PR → RG in AAQ62842. Ref.2
Sequence conflict477 – 4782RH → HY in CAA65529. Ref.1
Sequence conflict4861P → L in CAA65529. Ref.1
Sequence conflict6311R → C in CAA65529. Ref.1
Sequence conflict715 – 7173QGA → HST in CAA65529. Ref.1
Sequence conflict9421H → L in CAA65529. Ref.1
Sequence conflict12081R → E in CAA65529. Ref.1
Sequence conflict14051A → P in CAA65529. Ref.1
Sequence conflict15571R → P in CAA65529. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6UVK1 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 0B4F39AFC5ADD3CA

FASTA2,322250,537
        10         20         30         40         50         60 
MQSGPRPPLP APGLALALTL TMLARLASAA SFFGENHLEV PVATALTDID LQLQFSTSQP 

        70         80         90        100        110        120 
EALLLLAAGP ADHLLLQLYS GRLQVRLVLG QEELRLQTPA ETLLSDSIPH TVVLTVVEGW 

       130        140        150        160        170        180 
ATLSVDGFLN ASSAVPGAPL EVPYGLFVGG TGTLGLPYLR GTSRPLRGCL HAATLNGRSL 

       190        200        210        220        230        240 
LRPLTPDVHE GCAEEFSASD DVALGFSGPH SLAAFPAWGT QDEGTLEFTL TTQSRQAPLA 

       250        260        270        280        290        300 
FQAGGRRGDF IYVDIFEGHL RAVVEKGQGT VLLHNSVPVA DGQPHEVSVH INAHRLEISV 

       310        320        330        340        350        360 
DQYPTHTSNR GVLSYLEPRG SLLLGGLDAE ASRHLQEHRL GLTPEATNAS LLGCMEDLSV 

       370        380        390        400        410        420 
NGQRRGLREA LLTRNMAAGC RLEEEEYEDD AYGHYEAFST LAPEAWPAME LPEPCVPEPG 

       430        440        450        460        470        480 
LPPVFANFTQ LLTISPLVVA EGGTAWLEWR HVQPTLDLME AELRKSQVLF SVTRGARHGE 

       490        500        510        520        530        540 
LELDIPGAQA RKMFTLLDVV NRKARFIHDG SEDTSDQLVL EVSVTARVPM PSCLRRGQTY 

       550        560        570        580        590        600 
LLPIQVNPVN DPPHIIFPHG SLMVILEHTQ KPLGPEVFQA YDPDSACEGL TFQVLGTSSG 

       610        620        630        640        650        660 
LPVERRDQPG EPATEFSCRE LEAGSLVYVH RGGPAQDLTF RVSDGLQASP PATLKVVAIR 

       670        680        690        700        710        720 
PAIQIHRSTG LRLAQGSAMP ILPANLSVET NAVGQDVSVL FRVTGALQFG ELQKQGAGGV 

       730        740        750        760        770        780 
EGAEWWATQA FHQRDVEQGR VRYLSTDPQH HAYDTVENLA LEVQVGQEIL SNLSFPVTIQ 

       790        800        810        820        830        840 
RATVWMLRLE PLHTQNTQQE TLTTAHLEAT LEEAGPSPPT FHYEVVQAPR KGNLQLQGTR 

       850        860        870        880        890        900 
LSDGQGFTQD DIQAGRVTYG ATARASEAVE DTFRFRVTAP PYFSPLYTFP IHIGGDPDAP 

       910        920        930        940        950        960 
VLTNVLLVVP EGGEGVLSAD HLFVKSLNSA SYLYEVMERP RHGRLAWRGT QDKTTMVTSF 

       970        980        990       1000       1010       1020 
TNEDLLRGRL VYQHDDSETT EDDIPFVATR QGESSGDMAW EEVRGVFRVA IQPVNDHAPV 

      1030       1040       1050       1060       1070       1080 
QTISRIFHVA RGGRRLLTTD DVAFSDADSG FADAQLVLTR KDLLFGSIVA VDEPTRPIYR 

      1090       1100       1110       1120       1130       1140 
FTQEDLRKRR VLFVHSGADR GWIQLQVSDG QHQATALLEV QASEPYLRVA NGSSLVVPQG 

      1150       1160       1170       1180       1190       1200 
GQGTIDTAVL HLDTNLDIRS GDEVHYHVTA GPRWGQLVRA GQPATAFSQQ DLLDGAVLYS 

      1210       1220       1230       1240       1250       1260 
HNGSLSPRDT MAFSVEAGPV HTDATLQVTI ALEGPLAPLK LVRHKKIYVF QGEAAEIRRD 

      1270       1280       1290       1300       1310       1320 
QLEAAQEAVP PADIVFSVKS PPSAGYLVMV SRGALADEPP SLDPVQSFSQ EAVDTGRVLY 

      1330       1340       1350       1360       1370       1380 
LHSRPEAWSD AFSLDVASGL GAPLEGVLVE LEVLPAAIPL EAQNFSVPEG GSLTLAPPLL 

      1390       1400       1410       1420       1430       1440 
RVSGPYFPTL LGLSLQVLEP PQHGALQKED GPQARTLSAF SWRMVEEQLI RYVHDGSETL 

      1450       1460       1470       1480       1490       1500 
TDSFVLMANA SEMDRQSHPV AFTVTVLPVN DQPPILTTNT GLQMWEGATA PIPAEALRST 

      1510       1520       1530       1540       1550       1560 
DGDSGSEDLV YTIEQPSNGR VVLRGAPGTE VRSFTQAQLD GGLVLFSHRG TLDGGFRFRL 

      1570       1580       1590       1600       1610       1620 
SDGEHTSPGH FFRVTAQKQV LLSLKGSQTL TVCPGSVQPL SSQTLRASSS AGTDPQLLLY 

      1630       1640       1650       1660       1670       1680 
RVVRGPQLGR LFHAQQDSTG EALVNFTQAE VYAGNILYEH EMPPEPFWEA HDTLELQLSS 

      1690       1700       1710       1720       1730       1740 
PPARDVAATL AVAVSFEAAC PQRPSHLWKN KGLWVPEGQR ARITVAALDA SNLLASVPSP 

      1750       1760       1770       1780       1790       1800 
QRSEHDVLFQ VTQFPSRGQL LVSEEPLHAG QPHFLQSQLA AGQLVYAHGG GGTQQDGFHF 

      1810       1820       1830       1840       1850       1860 
RAHLQGPAGA SVAGPQTSEA FAITVRDVNE RPPQPQASVP LRLTRGSRAP ISRAQLSVVD 

      1870       1880       1890       1900       1910       1920 
PDSAPGEIEY EVQRAPHNGF LSLVGGGLGP VTRFTQADVD SGRLAFVANG SSVAGIFQLS 

      1930       1940       1950       1960       1970       1980 
MSDGASPPLP MSLAVDILPS AIEVQLRAPL EVPQALGRSS LSQQQLRVVS DREEPEAAYR 

      1990       2000       2010       2020       2030       2040 
LIQGPQYGHL LVGGRPTSAF SQFQIDQGEV VFAFTNFSSS HDHFRVLALA RGVNASAVVN 

      2050       2060       2070       2080       2090       2100 
VTVRALLHVW AGGPWPQGAT LRLDPTVLDA GELANRTGSV PRFRLLEGPR HGRVVRVPRA 

      2110       2120       2130       2140       2150       2160 
RTEPGGSQLV EQFTQQDLED GRLGLEVGRP EGRAPGPAGD SLTLELWAQG VPPAVASLDF 

      2170       2180       2190       2200       2210       2220 
ATEPYNAARP YSVALLSVPE AARTEAGKPE SSTPTGEPGP MASSPEPAVA KGGFLSFLEA 

      2230       2240       2250       2260       2270       2280 
NMFSVIIPMC LVLLLLALIL PLLFYLRKRN KTGKHDVQVL TAKPRNGLAG DTETFRKVEP 

      2290       2300       2310       2320 
GQAIPLTAVP GQGPPPGGQP DPELLQFCRT PNPALKNGQY WV 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of a human melanoma-associated chondroitin sulfate proteoglycan."
Pluschke G., Vanek M., Evans A., Dittmar T., Schmid P., Itin P., Filardo E.J., Reisfeld R.A.
Proc. Natl. Acad. Sci. U.S.A. 93:9710-9715(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Melanoma.
[2]"Melanoma chondroitin sulfate proteoglycan enhances FAK and ERK activation by distinct mechanisms."
Yang J., Price M.A., Neudauer C.L., Wilson C., Ferrone S., Xia H., Iida J., Simpson M.A., McCarthy J.B.
J. Cell Biol. 165:881-891(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Tissue: Melanoma.
[3]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"A role of chondroitin sulfate glycosaminoglycan binding site in alpha4beta1 integrin-mediated melanoma cell adhesion."
Iida J., Meijne A.M.L., Oegema T.R. Jr., Yednock T.A., Kovach N.L., Furcht L.T., McCarthy J.B.
J. Biol. Chem. 273:5955-5962(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITGA4.
[6]"Melanoma chondroitin sulphate proteoglycan regulates cell spreading through Cdc42, Ack-1 and p130cas."
Eisenmann K.M., McCarthy J.B., Simpson M.A., Keely P.J., Guan J.-L., Tachibana K., Lim L., Manser E., Furcht L.T., Iida J.
Nat. Cell Biol. 1:507-513(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BCAR1; CDC42 AND ACK1, FUNCTION.
[7]"Melanoma chondroitin sulfate proteoglycan regulates matrix metalloproteinase-dependent human melanoma invasion into type I collagen."
Iida J., Pei D., Kang T., Simpson M.A., Herlyn M., Furcht L.T., McCarthy J.B.
J. Biol. Chem. 276:18786-18794(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MMP16, FUNCTION.
[8]"A novel repeat in the melanoma-associated chondroitin sulfate proteoglycan defines a new protein family."
Staub E., Hinzmann B., Rosenthal A.
FEBS Lett. 527:114-118(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF CSPG REPEATS.
[9]"NG2 proteoglycan promotes endothelial cell motility and angiogenesis via engagement of galectin-3 and alpha3beta1 integrin."
Fukushi J., Makagiansar I.T., Stallcup W.B.
Mol. Biol. Cell 15:3580-3590(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITGA3; ITGB1 AND LGALS3.
[10]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2075.
Tissue: Plasma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X96753 mRNA. Translation: CAA65529.1.
AY359468 mRNA. Translation: AAQ62842.1.
AC105020 Genomic DNA. No translation available.
CH471136 Genomic DNA. Translation: EAW99239.1.
CH471136 Genomic DNA. Translation: EAW99240.1.
CCDSCCDS10284.1.
RefSeqNP_001888.2. NM_001897.4.
UniGeneHs.513044.

3D structure databases

ProteinModelPortalQ6UVK1.
SMRQ6UVK1. Positions 50-369.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107846. 5 interactions.
IntActQ6UVK1. 1 interaction.
MINTMINT-1197576.
STRING9606.ENSP00000312506.

PTM databases

PhosphoSiteQ6UVK1.

Polymorphism databases

DMDM296434468.

Proteomic databases

MaxQBQ6UVK1.
PaxDbQ6UVK1.
PRIDEQ6UVK1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308508; ENSP00000312506; ENSG00000173546.
GeneID1464.
KEGGhsa:1464.
UCSCuc002baw.3. human.

Organism-specific databases

CTD1464.
GeneCardsGC15M075966.
H-InvDBHIX0026925.
HIX0038117.
HIX0172852.
HIX0177623.
HIX0177624.
HGNCHGNC:2466. CSPG4.
HPACAB016189.
HPA002951.
MIM601172. gene.
neXtProtNX_Q6UVK1.
PharmGKBPA26963.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG261397.
HOGENOMHOG000170195.
HOVERGENHBG081360.
InParanoidQ6UVK1.
KOK08115.
OMARPIYRFT.
OrthoDBEOG77DJ56.
PhylomeDBQ6UVK1.
TreeFamTF316876.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SignaLinkQ6UVK1.

Gene expression databases

BgeeQ6UVK1.
CleanExHS_CSPG4.
GenevestigatorQ6UVK1.

Family and domain databases

Gene3D2.60.120.200. 2 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR001791. Laminin_G.
[Graphical view]
PfamPF02210. Laminin_G_2. 2 hits.
[Graphical view]
SMARTSM00282. LamG. 2 hits.
[Graphical view]
SUPFAMSSF49899. SSF49899. 2 hits.
PROSITEPS50025. LAM_G_DOMAIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCSPG4. human.
GeneWikiCSPG4.
GenomeRNAi1464.
NextBio6013.
PROQ6UVK1.
SOURCESearch...

Entry information

Entry nameCSPG4_HUMAN
AccessionPrimary (citable) accession number: Q6UVK1
Secondary accession number(s): D3DW77, Q92675
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM